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38 results about "Peptide mass" patented technology

In-gel tagging and in-gel digestion for phosphoproteins analysis and phosphorylation site identification

The present invention relates to a method for phosphorylation site-specific labeling of phosphoproteome with a site-specific tagging reagent and analyzing of the resulting labeled one, more especially, a method for in-situ tagging of phosphorylation sites of phosphoproteins retained in polymeric gel with a nucleophilic tagging reagent. It also relates a method for generating new proteolytic cleavable sites at formerly phosphorylation sites by a proper choice of a nucleophilic tagging reagent. It also relates to a method for phosphopeptides analysis and phosphorylation site identification by in-gel digestion of the previously in-gel tagged proteins and subsequent mass analysis of the resulting peptides. The invention provides in-gel chemical tagging method for phosphoaminoacid residue of phosphoproteins retained in polymeric gel matrix. Phosphoprotein can be immobilized into gel matrix by a variety of methods such as gel electrophoresis. The immobilized phosphoproteins are retained in gel matrix during tagging reaction to phosphorylated aminoacid residue of phosphoproteins, and the resulting tagged proteins are also retained in gel matrix till following purification steps like washing of the tagging reagents are accomplished. The tagged proteins is digested by protease, and the resulting digested peptides is released from gel into solution and applied for peptide mass analysis.
Owner:KOREA BASIC SCI INST

Stable isotope, site-specific mass tagging for protein identification

Proteolytic peptide mass mapping as measured by mass spectrometry provides an important method for the identification of proteins, which are usually identified by matching the measured and calculated m/z values of the proteolytic peptides. A unique identification is, however, heavily dependent upon the mass accuracy and sequence coverage of the fragment ions generated by peptide ionization. The present invention describes a method for increasing the specificity, accuracy and efficiency of the assignments of particular proteolytic peptides and consequent protein identification, by the incorporation of selected amino acid residue(s) enriched with stable isotope(s) into the protein sequence without the need for ultrahigh instrumental accuracy. Selected amino acid(s) are labeled with 13C/15N/2H and incorporated into proteins in a sequence-specific manner during cell culturing. Each of these labeled amino acids carries a defined mass change encoded in its monoisotopic distribution pattern. Through their characteristic patterns, the peptides with mass tag(s) can then be readily distinguished from other peptides in mass spectra. The present method of identifying unique proteins can also be extended to protein complexes and will significantly increase data search specificity, efficiency and accuracy for protein identifications.
Owner:LOS ALAMOS NATIONAL SECURITY

Stable isotope, site-specific mass tagging for protein identification

Proteolytic peptide mass mapping as measured by mass spectrometry provides an important method for the identification of proteins, which are usually identified by matching the measured and calculated m / z values of the proteolytic peptides. A unique identification is, however, heavily dependent upon the mass accuracy and sequence coverage of the fragment ions generated by peptide ionization. The present invention describes a method for increasing the specificity, accuracy and efficiency of the assignments of particular proteolytic peptides and consequent protein identification, by the incorporation of selected amino acid residue(s) enriched with stable isotope(s) into the protein sequence without the need for ultrahigh instrumental accuracy. Selected amino acid(s) are labeled with 13C / 15N / 2H and incorporated into proteins in a sequence-specific manner during cell culturing. Each of these labeled amino acids carries a defined mass change encoded in its monoisotopic distribution pattern. Through their characteristic patterns, the peptides with mass tag(s) can then be readily distinguished from other peptides in mass spectra. The present method of identifying unique proteins can also be extended to protein complexes and will significantly increase data search specificity, efficiency and accuracy for protein identifications.
Owner:LOS ALAMOS NATIONAL SECURITY

Identification method of highly stoichiometric non-germline mutation in eucaryotic cell

The invention relates to an identification method of the high stoichiometric ratio non-germline mutation in the eucaryotic cell and provides an semi-quantitative identification method of the protein synthesis error caused by the single amino acid mutation of the non-germline mutation (NGM), wherein the method is based on the proteomics technology and genome DNA sequencing of the mass spectrometry. The method is particularly as follows: the large-scale proteome analysis, the unrestricted sequence alignment and the identification and gene sequencing of the high resolution second-order mass spectrum and third-order mass spectrum of the synthetic peptide segment are integrated to perform systematic synthesis to the NGM and identify that the four peptide segments of four proteins contain the NGMs. By adopting the method for estimation, the NGM occurrence in the peptide segment is about 0.05%, which is more than 0.3% on the protein level. According to the peptide mass spectrum count ratio of mutant peptide segments to normal peptide segments, the stoichiometric ratio of the NGM is 0.05 to 0.71. By adopting the identification method, the NGM is proved to have high occurrence and stoichiometric ratio while the NGM is predicted to be used as a possible mechanism to join the basic biological and physiological processes.
Owner:JINGJIE PTM BIOLAB HANGZHOU CO LTD

In-Gel Tagging And In-Gel Digestion For Phosphoproteins Analysis And Phosphorylation Site Identification

The present invention relates to a method for phosphorylation site-specific labeling of phosphoproteome with a site-specific tagging reagent and analyzing of the resulting labeled one, more especially, a method for in-situ tagging of phosphorylation sites of phosphoproteins retained in polymeric gel with a nucleophilic tagging reagent. It also relates a method for generating new proteolytic cleavable sites at formerly phosphorylation sites by a proper choice of a nucleophilic tagging reagent. It also relates to a method for phosphopeptides analysis and phosphorylation site identification by in-gel digestion of the previously in-gel tagged proteins and subsequent mass analysis of the resulting peptides. The invention provides in-gel chemical tagging method for phosphoaminoacid residue of phosphoproteins retained in polymeric gel matrix. Phosphoprotein can be immobilized into gel matrix by a variety of methods such as gel electrophoresis. The immobilized phosphoproteins are retained in gel matrix during tagging reaction to phosphorylated aminoacid residue of phosphoproteins, and the resulting tagged proteins are also retained in gel matrix till following purification steps like washing of the tagging reagents are accomplished. The tagged proteins is digested by protease, and the resulting digested peptides is released from gel into solution and applied for peptide mass analysis.
Owner:KOREA BASIC SCI INST

Peptide-containing composition and stabilizer, stabilizing method, and storage method for peptide

The present invention provides novel technology for improving the storage stability of peptides such as glutathione. The present invention relates to a peptide-containing composition that comprises apeptide and an alkaline mineral carrier and in which there are 8 parts by mass of more of the alkaline mineral carrier with respect to 100 parts by mass of the peptide. The present invention also relates to a plant cultivation method that includes applying the peptide-containing composition to a plant. The present invention also relates to a stabilizer for a peptide, said stabilizer containing thealkaline mineral carrier. The present invention also relates to a method for improving the stability of a peptide, said method including a mixing step in which the alkaline mineral carrier is mixed with the peptide. The present invention also relates to a method for storing a peptide, said method including a storage step in which the peptide is stored together with the alkaline mineral carrier.
Owner:KANEKA CORP

Reagent for cutting sulfydryl-containing peptides from resins and cutting method

The invention relates to a reagent for cutting peptides, in particular to a reagent for cutting sulfydryl-containing peptides from resins. In addition, the invention also relates to a method for cutting sulfydryl-containing polypeptides from resins, which is suitable for industrial production of sulfydryl-containing polypeptides. The reagent for cutting sulfydryl-containing polypeptides from resins comprises the following components in parts by weight: 85-95 parts of trifluoroacetic acid, 1-5 parts of triisopropylsilane, 1-4 parts of mercaptoundecanoic acid, 1-4 parts of phenol and 1-2 parts of water. The invention has the advantages that because ethanedithiol is a chemical reagent which is not produced at home, the cost of the ethanedithiol is expensive, and the ethanedithiol has effluvial smell in the reaction process; in the invention, mercaptopropionic acid is used for replacing the conventional ethanedithiol, thus the production cost can be lowered, the environment pollution is greatly reduced, and simultaneously, the effect of the peptide cutting reaction can also be improved; and meanwhile, the invention has the characteristics of low procurement cost, reduction of the three wastes, good crude peptide quality and the like, and is very suitable for industrial production of sulfydryl-containing polypeptides.
Owner:SHANGHAI SOHO YIMING PHARMA
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